Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Identification of a family of human F-box proteins.
Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region.
Transforming activity of Fbxo7 is mediated specifically through regulation of cyclin D/cdk6.
Characterization of FBX25, encoding a novel brain-expressed F-box protein.
The F-box protein Fbxo7 interacts with human inhibitor of apoptosis protein cIAP1 and promotes cIAP1 ubiquitination.
Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor.
Loss of nuclear activity of the FBXO7 protein in patients with parkinsonian-pyramidal syndrome (PARK15).
A Competitive binding mechanism between Skp1 and exportin 1 (CRM1) controls the localization of a subset of F-box proteins.
Cyclin F-mediated degradation of ribonucleotide reductase M2 controls genome integrity and DNA repair.
FBXO7 immunoreactivity in α-synuclein-containing inclusions in Parkinson disease and multiple system atrophy.
The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy.
FBXO7 Y52C polymorphism as a potential protective factor in Parkinson's disease.
A proteome-scale map of the human interactome network.
Widespread macromolecular interaction perturbations in human genetic disorders.
F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
A High-Density Map for Navigating the Human Polycomb Complexome.
Architecture of the human interactome defines protein communities and disease networks.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degradation of UXT isoform 2 (UXT-V2) to inhibit the NF-κB signaling pathway.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
The SCF Complex Is Essential to Maintain Genome and Chromosome Stability.
E3 ligase adaptor FBXO7 contributes to ubiquitination and proteasomal degradation of SIRT7 and promotes cell death in response to hydrogen peroxide.
Multimodal cell maps as a foundation for structural and functional genomics.
AcM-UBE2M transfers NEDD8 to CRL1 E3 ubiquitin ligase complex
NEDD8:AcM-UBE2M binds CRL1 E3 ubiquitin ligase complex
CAND1 binds cytosolic CRL E3 ubiquitin ligases
COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes
COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes
MyrG-DCUN1D3 binds CRL1 E3 ubiquitin ligase complex
Transfer of Ub from E2 to substrate and release of E2
Release of E3 from polyubiquitinated substrate
Polyubiquitination of substrate
Interaction of E3 with substrate and E2-Ub complex
Falcon deep research report for human FBXO7
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FBXO7 is the substrate-recognition adaptor of an SCF-type E3 ubiquitin ligase, whose F-box domain binds SKP1 to link substrates to the CUL1-RBX1 catalytic core.
"FBXO7 is best understood as a **substrate-specifying adaptor** of an **SCF-type E3 ubiquitin ligase**, where its **F-box domain binds SKP1**, linking FBXO7 to the **CUL1–RBX1** catalytic core that recruits an E2~ubiquitin and transfers ubiquitin to substrates."
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FBXO7-driven ubiquitination is not exclusively degradative; it can generate K48-linked (proteasome-targeting) or K63-linked (non-proteolytic) chains depending on substrate and context.
"A key conceptual point is that **FBXO7-driven ubiquitination is not exclusively degradative**. It can generate **K48-linked polyubiquitin** (often proteasome-targeting) or **K63-linked chains** (often non-proteolytic signaling/trafficking/autophagy-related roles), depending on the substrate and context."
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Loss of Fbxo7 in mice reduces proteasome activity and produces a parkinsonism-like phenotype, supporting a role in neuronal proteostasis through proteasome assembly/composition tuning.
"In mouse models, **loss of Fbxo7** leads to **reduced proteasome activity** and a **parkinsonism-like phenotype**, supporting a role for FBXO7 in neuronal proteostasis."
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FBXO7 acts as a context-dependent tumor suppressor, catalyzing predominantly K48-linked polyubiquitination of INF2 (endometrial carcinoma, mitochondrial division control) and of PRMT1 (hepatocellular carcinoma, serine synthesis control).
"Together, these studies support FBXO7 as a context-dependent tumor suppressor via **mitochondrial homeostasis** and **amino-acid metabolism**, consistent with an E3 adaptor that tunes proteostasis, mitochondria, and stress responses."
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USP7 deubiquitinates and stabilizes FBXO7 by removing K48-linked ubiquitin chains, connecting deubiquitinase control of FBXO7 to cell survival under ER stress.
"USP7 deubiquitinates FBXO7 by removing **K48-linked ubiquitin chains**, preventing FBXO7 proteasomal degradation."